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UV/Vis Action Spectroscopy and Structures of Tyrosine Peptide Cation Radicals in the Gas Phase
Author(s) -
Viglino Emilie,
Shaffer Christopher J.,
Tureček František
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201602604
Subject(s) - chemistry , radical , intramolecular force , photochemistry , photodissociation , electron transfer , peptide , hydrogen atom abstraction , tyrosine , aromatic amino acids , spectroscopy , amino acid , stereochemistry , organic chemistry , biochemistry , physics , quantum mechanics
We report the first application of UV/Vis photodissociation action spectroscopy for the structure elucidation of tyrosine peptide cation radicals produced by oxidative intramolecular electron transfer in gas‐phase metal complexes. Oxidation of Tyr‐Ala‐Ala‐Ala‐Arg (YAAAR) produces Tyr‐O radicals by combined electron and proton transfer involving the phenol and carboxyl groups. Oxidation of Ala‐Ala‐Ala‐Tyr‐Arg (AAAYR) produces a mixture of cation radicals involving electron abstraction from the Tyr phenol ring and N‐terminal amino group in combination with hydrogen‐atom transfer from the C α positions of the peptide backbone.